ID   SYR_RHOBA               Reviewed;         671 AA.
AC   Q7URC7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=RB5747;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC         tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC         EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR   EMBL; BX294142; CAD74413.1; -; Genomic_DNA.
DR   RefSeq; NP_866872.1; NC_005027.1.
DR   RefSeq; WP_011120594.1; NC_005027.1.
DR   AlphaFoldDB; Q7URC7; -.
DR   SMR; Q7URC7; -.
DR   STRING; 243090.RB5747; -.
DR   EnsemblBacteria; CAD74413; CAD74413; RB5747.
DR   KEGG; rba:RB5747; -.
DR   PATRIC; fig|243090.15.peg.2764; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_0; -.
DR   InParanoid; Q7URC7; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
DR   InterPro; IPR005148; Arg-tRNA-synth_N.
DR   InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR   InterPro; IPR035684; ArgRS_core.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..671
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151598"
FT   REGION          223..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           124..134
FT                   /note="'HIGH' region"
SQ   SEQUENCE   671 AA;  74409 MW;  8AFF753698075DE8 CRC64;
     MHLPNVLQAR FVQALEPLTD SPSDYAGMIR PAADPKFGDY QSNAAMPLAK RVGKTSRDVA
     AELVQNLNVT DLFEEPEVAG PGFINLRLKD SVLFDSIQQM LLDERVGVSK TTDPKKVIVD
     FSSPNVAKPM HVGHIRSTVI GDCLARTLRF YGEDVVTDNH LGDWGTQFGI IIYGYRNFGD
     PAKVAANPVP ELSALYRLTN QLIEYQKAKQ SLATMADKLA TAKSDAKTAK EVSDQSESDE
     NLKPKDKKKL RKNAEAATRR VASIEADMKS LKAKIDAVDS DTELSKLASE HSDVDVAVLR
     ETAKLHEGDP ENLALWKEFL PHCQDEINRI YDRLNVQFDH TLGESFYHDR LAGVVDHLTT
     LGLTTKSDGA ICVFLEGFDS PMIIQKRDGA FLYATTDLAT LQYRRDEFQP DEILYVVDSR
     QGEHFKKFFA MAEPLGMAEV QLVHVNFGTV LGPDGRPMKT RSGSLIGLES LLNDAVSRAK
     EVVCNPDRLA TMDPPMGGEE QQQIAEIVGI GAIKYADLSH HRTSDYKFDV DKMVALEGNT
     ATYVQYSYAR TQSILRRASD GEGLPAFEQA IEQAAATQPM TFTHPNERSL ALMLMRFEEA
     IEQVRLNYAP NALCDYLFET AKTYSSFNES CRVLGNDDPA VMQTRLALVV LTGRVLKKGL
     SLLGIDVAER M
//